1dff: Difference between revisions
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|PDB= 1dff |SIZE=350|CAPTION= <scene name='initialview01'>1dff</scene>, resolution 2.88Å | |PDB= 1dff |SIZE=350|CAPTION= <scene name='initialview01'>1dff</scene>, resolution 2.88Å | ||
|SITE= <scene name='pdbsite=CAT:Zn+Binding+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Zn+Binding+Site'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dff OCA], [http://www.ebi.ac.uk/pdbsum/1dff PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dff RCSB]</span> | |||
}} | }} | ||
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[[Category: Rajagopalan, P T.R.]] | [[Category: Rajagopalan, P T.R.]] | ||
[[Category: Tsai, C M.]] | [[Category: Tsai, C M.]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: zinc metalloprotease]] | [[Category: zinc metalloprotease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:40:32 2008'' | ||
Revision as of 19:40, 30 March 2008
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| , resolution 2.88Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Formylmethionine deformylase, with EC number 3.5.1.31 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEPTIDE DEFORMYLASE
OverviewOverview
Protein synthesis in bacteria involves the formylation and deformylation of the N-terminal methionine. As eukaryotic organisms differ in their protein biosynthetic mechanisms, peptide deformylase, the bacterial enzyme responsible for deformylation, represents a potential target for antibiotic studies. Here we report the crystallization and 2.9 A X-ray structure solution of the zinc containing Escherichia coli peptide deformylase. While the primary sequence, tertiary structure, and use of coordinated cysteine suggest that E. coli deformylase belongs to a new subfamily of metalloproteases, the environment around the metal appears to have strong geometric similarity to the active sites of the thermolysin family. This suggests a possible similarity in their hydrolytic mechanisms. Another important issue is the origin of the enzyme's specificity for N-formylated over N-acetylated substrates. Based on the structure, the specificity appears to result from hydrogen-bonding interactions which orient the substrate for cleavage, and steric factors which physically limit the size of the N-terminal carbonyl group.
About this StructureAbout this Structure
1DFF is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the Escherichia coli peptide deformylase., Chan MK, Gong W, Rajagopalan PT, Hao B, Tsai CM, Pei D, Biochemistry. 1997 Nov 11;36(45):13904-9. PMID:9374869
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